CISD2_LITCT
ID CISD2_LITCT Reviewed; 135 AA.
AC C1C524;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=CDGSH iron-sulfur domain-containing protein 2;
GN Name=cisd2;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Helbing C.C., Veldhoen N., Leong J., Koop B.F.;
RT "Rana catesbeiana ESTs and full-length cDNAs.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of autophagy that contributes to antagonize becn1-
CC mediated cellular autophagy at the endoplasmic reticulum. Participates
CC in the interaction of bcl2 with becn1 and is required for bcl2-mediated
CC depression of endoplasmic reticulum Ca(2+) stores during autophagy (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Mitochondrion outer
CC membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CISD protein family. CISD2 subfamily.
CC {ECO:0000305}.
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DR EMBL; BT081953; ACO52084.1; -; mRNA.
DR AlphaFoldDB; C1C524; -.
DR SMR; C1C524; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR Gene3D; 3.40.5.90; -; 1.
DR InterPro; IPR045131; CISD1/2.
DR InterPro; IPR018967; FeS-contain_CDGSH-typ.
DR InterPro; IPR019610; FeS-contain_mitoNEET_N.
DR InterPro; IPR042216; MitoNEET_CISD.
DR PANTHER; PTHR13680; PTHR13680; 1.
DR Pfam; PF10660; MitoNEET_N; 1.
DR Pfam; PF09360; zf-CDGSH; 1.
DR SMART; SM00704; ZnF_CDGSH; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Autophagy; Endoplasmic reticulum; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..135
FT /note="CDGSH iron-sulfur domain-containing protein 2"
FT /id="PRO_0000392018"
FT TOPO_DOM 1..37
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
SQ SEQUENCE 135 AA; 15410 MW; AA7652F491831FB2 CRC64;
MVLEILARVI KVQLPAYLKR LPVPDSIAGF IRLTVSEWLR LLPFLGVLAL LGYLAIRPFL
PKKKQQKDSL INLKIQKENP KVVNEIDIED LRIAKVAYCR CWRSKTFPVC DGSHNKHNEL
TGDNVGPLIL KKKEV
